4G2V

Structure complex of LGN binding with FRMPD1

Summary for 4G2V

• Entry DOI: 10.2210/pdb4g2v/pdb
• Descriptor: G-protein-signaling modulator 2, peptide from FERM and PDZ domain-containing protein 1, GLYCEROL, ... (6 entities in total)
• Functional Keywords: tpr repeat, lgn, cell polarity, protein binding
• Biological source: Mus musculus (mouse); More
• Cellular location: Cytoplasm (By similarity): Q8VDU0; Cytoplasm, cytosol: Q5SYB0
• Total number of polymer chains: 2
• Total formula weight: 42673.12

Authors

Shang, Y.,Pan, Z.,Wen, W.,Wang, W.,Zhang, M. (deposition date: 2012-07-13, release date: 2013-01-23, Last modification date: 2024-03-20)

Primary citation

Pan, Z.,Shang, Y.,Jia, M.,Zhang, L.,Xia, C.,Zhang, M.,Wang, W.,Wen, W.
Structural and biochemical characterization of the interaction between LGN and Frmpd1
J.Mol.Biol., 425:1039-1049, 2013

PubMed Abstract: The tetratricopeptide repeat (TPR) motif-containing protein LGN binds multiple targets and regulates their subcellular localizations and functions during both asymmetric and symmetric cell divisions. Here, we characterized the interaction between LGN-TPR motifs and FERM and PDZ domain containing 1 (Frmpd1) and reported the crystal structure of the complex at 2.4Å resolution. A highly conserved fragment at the center of Frmpd1 of ~20 residues was found to be necessary and sufficient to bind to LGN-TPR. This Frmpd1 fragment forms an extended structure and runs along the concave channel of the TPR superhelix in an antiparallel manner in the complex. Structural comparisons and biochemical studies of LGN/Frmpd1 and other known LGN/target interactions demonstrate that the LGN-TPR motifs are versatile and capable of recognizing multiple targets via diverse binding modes. Nevertheless, a conserved "E/QxEx4-5E/D/Qx1-2K/R" motif in LGN/Pins (partner of inscuteable) TPR binding proteins has been identified.

PubMed: 23318951
DOI: 10.1016/j.jmb.2013.01.003

Experimental method

X-RAY DIFFRACTION (2.4 Å)